Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition
Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself. According to the literature, GroEL reassembly is dependent on chaperonin ligands and solvent composition. He...
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doaj-f550c5dbf58a4dc59d6b2641e06538a52020-11-25T00:40:17ZengMDPI AGBiomolecules2218-273X2014-04-014245847310.3390/biom4020458biom4020458Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent CompositionNataliya Ryabova0Victor Marchenkov1Nina Kotova2Gennady Semisotnov3Institute of Protein Research, Russian Academy of Sciences, Institutskaya Street 4, Pushchino 142290, RussiaInstitute of Protein Research, Russian Academy of Sciences, Institutskaya Street 4, Pushchino 142290, RussiaInstitute of Protein Research, Russian Academy of Sciences, Institutskaya Street 4, Pushchino 142290, RussiaInstitute of Protein Research, Russian Academy of Sciences, Institutskaya Street 4, Pushchino 142290, RussiaChaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself. According to the literature, GroEL reassembly is dependent on chaperonin ligands and solvent composition. Here we demonstrate dependence of GroEL reassembly efficiency on concentrations of the essential factors (Mg2+, ADP, ATP, GroES, ammonium sulfate, NaCl and glycerol). Besides, kinetics of GroEL oligomerization in various conditions was monitored by the light scattering technique and proved to be two-exponential, which suggested accumulation of a certain oligomeric intermediate. This intermediate was resolved as a heptamer by nondenaturing blue electrophoresis of GroEL monomers during their assembly in the presence of both Mg-ATP and co-chaperonin GroES. Presumably, this intermediate heptamer plays a key role in formation of the GroEL tetradecameric particle. The role of co-chaperonin GroES (Hsp10) in GroEL assembly is also discussed.http://www.mdpi.com/2218-273X/4/2/458oligomeric protein foldingchaperonin GroELdenaturationreassembly |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Nataliya Ryabova Victor Marchenkov Nina Kotova Gennady Semisotnov |
spellingShingle |
Nataliya Ryabova Victor Marchenkov Nina Kotova Gennady Semisotnov Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition Biomolecules oligomeric protein folding chaperonin GroEL denaturation reassembly |
author_facet |
Nataliya Ryabova Victor Marchenkov Nina Kotova Gennady Semisotnov |
author_sort |
Nataliya Ryabova |
title |
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition |
title_short |
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition |
title_full |
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition |
title_fullStr |
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition |
title_full_unstemmed |
Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition |
title_sort |
chaperonin groel reassembly: an effect of protein ligands and solvent composition |
publisher |
MDPI AG |
series |
Biomolecules |
issn |
2218-273X |
publishDate |
2014-04-01 |
description |
Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself. According to the literature, GroEL reassembly is dependent on chaperonin ligands and solvent composition. Here we demonstrate dependence of GroEL reassembly efficiency on concentrations of the essential factors (Mg2+, ADP, ATP, GroES, ammonium sulfate, NaCl and glycerol). Besides, kinetics of GroEL oligomerization in various conditions was monitored by the light scattering technique and proved to be two-exponential, which suggested accumulation of a certain oligomeric intermediate. This intermediate was resolved as a heptamer by nondenaturing blue electrophoresis of GroEL monomers during their assembly in the presence of both Mg-ATP and co-chaperonin GroES. Presumably, this intermediate heptamer plays a key role in formation of the GroEL tetradecameric particle. The role of co-chaperonin GroES (Hsp10) in GroEL assembly is also discussed. |
topic |
oligomeric protein folding chaperonin GroEL denaturation reassembly |
url |
http://www.mdpi.com/2218-273X/4/2/458 |
work_keys_str_mv |
AT nataliyaryabova chaperoningroelreassemblyaneffectofproteinligandsandsolventcomposition AT victormarchenkov chaperoningroelreassemblyaneffectofproteinligandsandsolventcomposition AT ninakotova chaperoningroelreassemblyaneffectofproteinligandsandsolventcomposition AT gennadysemisotnov chaperoningroelreassemblyaneffectofproteinligandsandsolventcomposition |
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1725291195842691072 |